- Protein Classification
- Protein Links
 | perinuclear space side |
| cytoplasmic side |
| 1cjy » Cytosolic phospholipase A2, group IVA | |
|---|---|
| Depth | 5.8 ± 1.0 Å |
| Tilt Angle | 70 ± 9° |
| ΔGtransfer | -9.9 kcal/mol |
| Links to 1cjy | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | cytoplasmic |
| Resolution | 2.5 Å |
| Other PDB entries of this protein | 1bci, 1rlw |
| Number of subunits | 1 |
| Experimental Verification for 1cjy » Cytosolic phospholipase A2, group IVA |
|---|
| Mutations of residues I399, L400 and L552 slightly affect membrane binding (Das and Cho 2002). However, these residues are completely buried in the protein interior. This is probably an indirect effect (authors suggest conformational changes). Maximal membrane binding afinity: -11 kcal/mol (Stahelin and Cho 2001). |
| 2 references |
|---|
| Das S, Cho W. 2002. Roles of catalytic domain residues in interfacial binding and activation of group IV cytosolic phospholipase A2. J Biol Chem. 277:23838-46. PubMed |
| Stahelin RV, Cho W. 2001. Roles of calcium ions in the membrane binding of C2 domains. Biochem J. 359:679-85. PubMed |
| Comments on 1cjy » Cytosolic phospholipase A2, group IVA |
|---|
| Orientation of an isolated C2 domain (1rlw) is nearly the same. Patatin and catalytic domain of cPLA have clear sequence identity, despite of the numerous structural differences. |
